How do proteins fold into their unique three-dimensional structures? How does the three dimensional structure of a protein give rise to function? Can proteins be designed, either from first principles or through reconstruction of natural protein substructures? Can low molecular weight and highly stable mimics of natural proteins be designed? This meeting will describe progress towards understanding these questions that lie at the heart of modern molecular biology. In-recent years folding motifs have been recognized in a variety of gene regulatory proteins, and their structures are being determined by a combination of predictive methods, NMR, and crystallography. Considerable progress with the folding problem has been made in vitro studies as well as whole cells. Enormous progress has been made in understanding the structures and functions of membrane proteins. We have begun to study and manipulate the repertoire of biological molecular recognition using immunoglobulins and related molecules. This meeting should bring together chemists, molecular biologists, and cellular biologists to review recent advances in these areas, and discuss the future of this multidisciplinary field.